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Title: Lysozyme net charge and ion binding in concentrated aqueous electrolyte solutions

Journal Article · · Journal of Physical Chemistry B: Materials, Surfaces, Interfaces, amp Biophysical
DOI:https://doi.org/10.1021/jp983852i· OSTI ID:347556
; ; ; ;  [1];  [1]
  1. Univ. of California, Berkeley, CA (United States). Dept. of Chemical Engineering

Hydrogen-ion titrations were conducted for hen-egg-white lysozyme in solutions of potassium chloride over the range pH 2.5--11.5 and for ionic strengths to 2.0 M. The dependence of lysozyme`s net proton charge, z{sub p}, on pH and ionic strength in potassium chloride solution is measured. From the ionic-strength dependence of z{sub p}, interactions of lysozyme with potassium and chloride ions are calculated using the molecular-thermodynamic theory of Fraaije and Lyklema. Lysozyme interacts preferentially with up to 12 chloride ions at pH 2.5. The observed dependence of ion-protein interactions on pH and ionic strength is explained in terms of electric-double-layer theory. New experimental pK{sub a} data are reported for 11 amino acids in potassium chloride solutions of ionic strength to 3.0 M.

Research Organization:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC03-76SF00098
OSTI ID:
347556
Report Number(s):
LBNL-42717; ISSN 1089-5647; TRN: IM9923%%93
Journal Information:
Journal of Physical Chemistry B: Materials, Surfaces, Interfaces, amp Biophysical, Vol. 103, Issue 8; Other Information: PBD: 25 Feb 1999
Country of Publication:
United States
Language:
English

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